{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T06:34:19Z","timestamp":1779345259483,"version":"3.51.4"},"reference-count":66,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[1995,2,1]],"date-time":"1995-02-01T00:00:00Z","timestamp":791596800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,17]],"date-time":"2013-07-17T00:00:00Z","timestamp":1374019200000},"content-version":"vor","delay-in-days":6741,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Structure"],"published-print":{"date-parts":[[1995,2]]},"DOI":"10.1016\/s0969-2126(01)00147-2","type":"journal-article","created":{"date-parts":[[2004,7,23]],"date-time":"2004-07-23T19:10:35Z","timestamp":1090609835000},"page":"163-176","source":"Crossref","is-referenced-by-count":102,"title":["The crystal structure of the lysyl-tRNA synthetase (LysU) from Escherichia coli"],"prefix":"10.1016","volume":"3","author":[{"given":"Silvia","family":"Onesti","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andrew D","family":"Miller","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peter","family":"Brick","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/S0969-2126(01)00147-2_BIB1","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1038\/347203a0","article-title":"Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs","volume":"347","author":"Eriani","year":"1990","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB2","doi-asserted-by":"crossref","first-page":"8121","DOI":"10.1073\/pnas.88.18.8121","article-title":"Evolution and relatedness in two aminoacyl-tRNA synthetase families","volume":"88","author":"Nagel","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB3","doi-asserted-by":"crossref","first-page":"3489","DOI":"10.1093\/nar\/19.13.3489","article-title":"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases","volume":"19","author":"Cusack","year":"1991","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB4","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/0022-2836(89)90090-9","article-title":"Structure of tyrosyl-tRNA synthetase refined at 2.3 \u00e5 resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate","volume":"208","author":"Brick","year":"1988","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB5","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1126\/science.2479982","article-title":"Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNAGln and ATP at 2.8 \u00e5 resolution","volume":"246","author":"Rould","year":"1989","journal-title":"Science"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB6","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/S0022-2836(05)80331-6","article-title":"Crystallographic study at 2.5 \u00e5 resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP","volume":"216","author":"Brunie","year":"1990","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB7","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1107\/S0108767393010037","article-title":"Overcoming non-isomorphism by phase permutation and likelihood scoring \u2014solution of the TrpRS crystal structure","volume":"50","author":"Doublie","year":"1994","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB8","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1038\/347249a0","article-title":"A 2nd class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-transfer RNA synthetase at 2.5 \u00e5","volume":"347","author":"Cusack","year":"1990","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB9","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1006\/jmbi.1993.1576","article-title":"Refined structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 \u00e5 resolution","volume":"234","author":"Fujinaga","year":"1993","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB10","doi-asserted-by":"crossref","first-page":"1682","DOI":"10.1126\/science.2047877","article-title":"Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNAAsp","volume":"252","author":"Ruff","year":"1991","journal-title":"Science"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB11","doi-asserted-by":"crossref","first-page":"3219","DOI":"10.1002\/j.1460-2075.1994.tb06623.x","article-title":"Crystal structure of a prokaryotic aspartyl-tRNA synthetase","volume":"13","author":"Delarue","year":"1994","journal-title":"EMBO J"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB12","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1016\/0300-9084(93)90008-G","article-title":"Phenylalanyl-tRNA synthetase from Thermus thermophilus has four antiparallel folds of which only two are catalytically functional","volume":"75","author":"Mosyak","year":"1993","journal-title":"Biochimie"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB13","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1006\/jmbi.1994.1547","article-title":"Crystallization of the glycyl-tRNA synthetase from Thermus thermophilus and initial crystallographic data","volume":"241","author":"Logan","year":"1994","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB14","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1006\/jmbi.1994.1498","article-title":"Crystallization of histidyl-tRNA synthetase from Escherichia coli.","volume":"241","author":"Francklyn","year":"1994","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB15","series-title":"Biological Macromolecules and Assemblies vol 2","first-page":"442","article-title":"Aminoacyl-tRNA synthetases","author":"Blow","year":"1985"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB16","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/0968-0004(92)90326-5","article-title":"Structural and functional relationships between aminoacyl-tRNA synthetases","volume":"17","author":"Moras","year":"1992","journal-title":"Trends Biochem. Sci"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB17","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1038\/nsb1194-758","article-title":"A tale of two synthetases","volume":"1","author":"Artymiuk","year":"1994","journal-title":"Nat. Struct. Biol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB18","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1038\/362181a0","article-title":"Yeast tRNAAsp recognition by its cognate class II aminoacyl-tRNA synthetase","volume":"362","author":"Cavarelli","year":"1993","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB19","doi-asserted-by":"crossref","first-page":"1404","DOI":"10.1126\/science.8128220","article-title":"The 2.9 \u00e5 crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNASer","volume":"263","author":"Biou","year":"1994","journal-title":"Science"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB20","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1093\/nar\/18.2.305","article-title":"Homology of lysS and lysU, the two Escherichia coli genes encoding distinct lysyl-tRNA synthetase species","volume":"18","author":"L\u00e9v\u00e9que","year":"1990","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB21","doi-asserted-by":"crossref","first-page":"3237","DOI":"10.1128\/jb.172.6.3237-3243.1990","article-title":"Role of the two lysyl-tRNA synthetases of Escherichia coli: analysis of nucleotide sequences and mutant behaviour","volume":"172","author":"Clark","year":"1990","journal-title":"J. Bacteriol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB22","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1128\/JB.158.2.615-620.1984","article-title":"Escherichia coli K-12 lysyl-tRNA synthetase mutant with a novel reversion pattern","volume":"158","author":"Hirshfield","year":"1984","journal-title":"J. Bacteriol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB23","doi-asserted-by":"crossref","first-page":"1739","DOI":"10.1111\/j.1365-2958.1992.tb01346.x","article-title":"Differential regulation of two genes encoding lysyl-tRNA synthetases in Escherichia coli: lysU-constitutive mutations compensate for a lysS null mutation","volume":"6","author":"Kawakami","year":"1992","journal-title":"Mol. Microbiol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB24","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/0092-8674(84)90318-0","article-title":"AppppA and related adenylated nucleotides are synthesized as a consequence of oxidation stress","volume":"37","author":"Bochner","year":"1984","journal-title":"Cell"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB25","doi-asserted-by":"crossref","first-page":"7496","DOI":"10.1073\/pnas.80.24.7496","article-title":"AppppA, heat-shock stress and cell oxidation","volume":"80","author":"Lee","year":"1983","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB26","doi-asserted-by":"crossref","first-page":"2350","DOI":"10.1073\/pnas.83.8.2350","article-title":"Alteration of adenyl dinucleotide metabolism by environmental stress","volume":"83","author":"Baker","year":"1986","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB27","doi-asserted-by":"crossref","first-page":"3897","DOI":"10.1002\/j.1460-2075.1991.tb04959.x","article-title":"AppppA binds to several proteins in Escherichia coli, including the heat-shock and oxidative stress proteins DnaK, GroEL, E89, C45 and C40","volume":"10","author":"Johnstone","year":"1991","journal-title":"EMBO J"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB28","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1128\/jb.168.2.931-935.1986","article-title":"Escherichia coli DnaK protein possesses a 5\u2032-nucleotidase activity that is inhibited by AppppA","volume":"168","author":"Bochner","year":"1986","journal-title":"J. Bacteriol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB29","doi-asserted-by":"crossref","first-page":"2321","DOI":"10.1128\/jb.175.8.2321-2326.1993","article-title":"Apppp-binding protein E89 is the Escherichia coli heat-shock protein ClpB","volume":"175","author":"Fuge","year":"1993","journal-title":"J. Bacteriol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB30","doi-asserted-by":"crossref","first-page":"8275","DOI":"10.1073\/pnas.86.21.8275","article-title":"In vivo synthesis of adenylated bis (5-nucleosidyl) tetraphosphates (Ap4N) by Escherichia coli aminoacyl-tRNA synthetases","volume":"89","author":"Brevet","year":"1989","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB31","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1039\/C39940000659","article-title":"Enzymatic synthesis of diadenosine 5\u2032,5\u2034-P1, P4-tetraphosphates (Ap4A) analogues by stress protein LysU","volume":"5","author":"Theoclitou","year":"1994","journal-title":"J. Chem. Soc. Chem. Commun"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB32","doi-asserted-by":"crossref","first-page":"5273","DOI":"10.1021\/bi00264a024","article-title":"Zinc-dependent synthesis of various dinucleoside 5\u2032,5\u2034-P1, P3-tri-\u00a0or 5\u2032,5\u2034-P1, P4-tetraphosphates by Escherichia coli lysyl-tRNA synthetase","volume":"21","author":"Plateau","year":"1982","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB33","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1016\/0020-711X(89)90200-0","article-title":"Diadenosine tetraphosphate (Ap4A): its presence and functions in biological systems","volume":"21","author":"Andersson","year":"1989","journal-title":"Int. J. Biochem"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB34","doi-asserted-by":"crossref","first-page":"5286","DOI":"10.1016\/S0021-9258(18)89019-6","article-title":"Synthesis of diadenosine 5\u2032,5\u2034-P1, P4-tetraphosphate by lysyl-tRNA synthetase and a multienzyme complex of aminoacyl-tRNA synthetases from rat liver","volume":"260","author":"Wahab","year":"1985","journal-title":"J. Biol. Chem"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB35","doi-asserted-by":"crossref","first-page":"1586","DOI":"10.1021\/bi00380a015","article-title":"A preferential role for lysyl-tRNA4 in the synthesis of diadenosine 5\u2032,5\u2034-P1, P4-tetraphosphates by an arginyl tRNA synthetase lysyl-tRNA synthetase complex from rat liver","volume":"26","author":"Hilderman","year":"1987","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB36","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1016\/0014-5793(92)80857-D","article-title":"Escherichia coli leucine responsive regulatory protein (Lrp) controls lysyl-tRNA synthetase expression","volume":"300","author":"Gazeau","year":"1992","journal-title":"FEBS Lett"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB37","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1006\/jmbi.1994.1514","article-title":"Structure\u2013function relationship of the trp-binding region upstream of lysU in Escherichia coli.","volume":"241","author":"Gazeau","year":"1992","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB38","doi-asserted-by":"crossref","first-page":"2779","DOI":"10.1128\/jb.174.9.2779-2784.1992","article-title":"The lrp gene product regulates expression of lysU in Escherichia coli K-12","volume":"174","author":"Lin","year":"1992","journal-title":"J. Bacteriol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB39","doi-asserted-by":"crossref","first-page":"7903","DOI":"10.1128\/jb.173.24.7903-7910.1991","article-title":"Control of Escherichia coli lysyl-tRNA synthetase expression by anaerobiosis","volume":"173","author":"L\u00e9v\u00e9que","year":"1991","journal-title":"J. Bacteriol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB40","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1006\/jmbi.1994.1635","article-title":"Crystallization and preliminary diffraction studies of E. coli lysyl-tRNA synthetase (LysU)","volume":"243","author":"Onesti","year":"1994","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB41","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1002\/bip.360221211","article-title":"Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features","volume":"22","author":"Kabsch","year":"1983","journal-title":"Biopolymers"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB42","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1016\/S0006-3495(65)86759-5","article-title":"Stereochemical criteria for polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide units","volume":"5","author":"Ramakrishman","year":"1965","journal-title":"Biophys. J"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB43","doi-asserted-by":"crossref","first-page":"1321","DOI":"10.1021\/bi00327a009","article-title":"A peculiar property of aspartyl-tRNA synthetase from baker\u2019s yeast: chemical modification of the protein by the enzymatically synthesized aminoacyl adenylate","volume":"24","author":"Kern","year":"1985","journal-title":"Biochemistry"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB44","doi-asserted-by":"crossref","first-page":"10816","DOI":"10.1073\/pnas.90.22.10816","article-title":"Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline","volume":"90","author":"Eriani","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB45","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1002\/prot.340100203","article-title":"The crystal structure of Staphylococcal nuclease refined to 1.7 \u00e5 resolution","volume":"10","author":"Hynes","year":"1991","journal-title":"Proteins"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB46","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1038\/355561a0","article-title":"Lactose binding to heat-labile enterotoxin revealed by X-ray crystallography","volume":"355","author":"Sixma","year":"1992","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB47","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1002\/j.1460-2075.1993.tb05726.x","article-title":"OB (oligonucleotide\/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences","volume":"12","author":"Murzin","year":"1993","journal-title":"EMBO J"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB48","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1016\/0022-2836(91)90701-7","article-title":"Structure and evolution of a group of related aminoacyl-tRNA synthetases","volume":"218","author":"Gatti","year":"1991","journal-title":"J. Mol. Biol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB49","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1016\/0092-8674(92)90433-D","article-title":"Autoregulation of the yeast lysyl-tRNA synthetase gene GCD5\/KRS1 by translational and transcriptional control mechanisms","volume":"70","author":"Lanker","year":"1992","journal-title":"Cell"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB50","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1002\/j.1460-2075.1994.tb06265.x","article-title":"The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction","volume":"13","author":"Cavarelli","year":"1994","journal-title":"EMBO J"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB51","doi-asserted-by":"crossref","first-page":"1432","DOI":"10.1126\/science.8128224","article-title":"Crystal structure at 2.5 \u00e5 resolution of seryl-tRNA synthetase complexed with two analogs of seryl adenylate","volume":"263","author":"Belrhali","year":"1994","journal-title":"Science"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB52","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1107\/S002188988708662X","article-title":"Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography","volume":"20","author":"Messerschmidt","year":"1987","journal-title":"J. Appl. Crystallogr"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB53","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1107\/S0108767387099720","article-title":"A reciprocal-space method for calculating a molecular envelope using the algorithm of B.C. Wang","volume":"43","author":"Leslie","year":"1987","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB54","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 suite: programs for protein crystallography","volume":"50","author":"Collaborative Computational Project, Number 4","year":"1994","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB55","series-title":"Proceedings of the CCP4 Study Weekend: Isomorphous Replacement and Anomalous Scattering","first-page":"23","article-title":"Heavy atom location using SHELXS-90","author":"Sheldrick","year":"1991"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB56","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1107\/S0108767386099622","article-title":"Improved Fourier coefficients for maps using phases from partial structures with errors","volume":"42","author":"Read","year":"1986","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB57","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1016\/0076-6879(85)15017-2","article-title":"Computer skeletonization and automatic electron-density map analysis","volume":"115","author":"Greer","year":"1985","journal-title":"Methods Enzymol"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB58","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1107\/S0108767390010224","article-title":"Improved methods for building protein models in electron density maps and the location of errors in these models","volume":"47","author":"Jones","year":"1991","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB59","series-title":"Proceedings of the CCP4 Study Weekend: From First Map to Final Model","first-page":"59","article-title":"Halloween \u2026 masks and bones","author":"Kleywegt","year":"1994"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB60","first-page":"1","article-title":"Making the first trace with O","author":"Jones","year":"1994","journal-title":"Proceeding of the CCP4 study weekend: From First Map to Final Model"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB61","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1002\/j.1460-2075.1986.tb04287.x","article-title":"Using known substructures in protein model building and crystallography","volume":"5","author":"Jones","year":"1986","journal-title":"EMBO J"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB62","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1126\/science.235.4787.458","article-title":"Crystallographic R-factor refinement by molecular dynamics","volume":"235","author":"Brunger","year":"1987","journal-title":"Science"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB63","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1107\/S0108767391001071","article-title":"Accurate bond angle and parameters for X-ray protein structure refinement","volume":"45","author":"Engh","year":"1991","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB64","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1038\/355472a0","article-title":"The free R value: a novel statistical quantity for assessing the accuracy of crystal structures","volume":"355","author":"Brunger","year":"1992","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB65","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1107\/S0021889891004399","article-title":"MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures","volume":"24","author":"Kraulis","year":"1991","journal-title":"J. Appl. Crystallogr"},{"key":"10.1016\/S0969-2126(01)00147-2_BIB66","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/S0263-7855(98)80030-1","article-title":"A fast algorithm for rendering space filling molecule pictures","volume":"6","author":"Bacon","year":"1988","journal-title":"J. Mol. Graphics"}],"container-title":["Structure"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212601001472?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212601001472?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,6,24]],"date-time":"2021-06-24T14:39:29Z","timestamp":1624545569000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0969212601001472"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,2]]},"references-count":66,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1995,2]]}},"alternative-id":["S0969212601001472"],"URL":"https:\/\/doi.org\/10.1016\/s0969-2126(01)00147-2","relation":{},"ISSN":["0969-2126"],"issn-type":[{"value":"0969-2126","type":"print"}],"subject":[],"published":{"date-parts":[[1995,2]]}}}